Biology:Biotin—(acetyl-CoA-carboxylase) ligase
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Short description: Enzyme
| Biotin—[acetyl-CoA-carboxylase] ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.4.15 | ||||||||
| CAS number | 37340-95-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a biotin—[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15) is an enzyme that catalyzes the chemical reaction
- ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] [math]\displaystyle{ \rightleftharpoons }[/math] AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
The 3 substrates of this enzyme are ATP, biotin, and apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)], whereas its 3 products are AMP, diphosphate, and acetyl-CoA:carbon-dioxide ligase (ADP-forming).
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds.
This enzyme participates in biotin metabolism. This protein may use the morpheein model of allosteric regulation.[1]
Nomenclature
The systematic name of this enzyme class is biotin:apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming). Other names in common use include:
- biotin-[acetyl-CoA carboxylase] synthetase,
- biotin-[acetyl coenzyme A carboxylase] synthetase,
- acetyl coenzyme A holocarboxylase synthetase,
- acetyl CoA holocarboxylase synthetase,
- biotin:apocarboxylase ligase,
- biotin holoenzyme synthetase,
- and HCS.
References
- ↑ "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. March 2012. doi:10.1016/j.abb.2011.11.020. PMID 22182754.
Further reading
- "Acetyl-Coenzyme A carboxylase. Role of the prosthetic group in enzyme polymerization". Biochem. J. 145 (3): 545–8. March 1975. doi:10.1042/bj1450545. PMID 239688.
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